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The Myc/Max/Mad network comprises a group of transcription factors that co-interact to regulate gene-specific transcriptional activation or repression. Additionally we are shipping MNT Antibodies (25) and and many more products for this protein.
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results redefine the physiological relationship between Mnt and Myc (show MYC Proteins) and requirements for Myc (show MYC Proteins)-driven oncogenesis
Mxd4 (show MXD4 Proteins) and Mnt upregulation following OX40 (show TNFRSF4 Proteins) engagement most likely increases T-cell survival
There is a unique negative regulatory role for Mnt in governing key Myc (show MYC Proteins) functions associated with cell proliferation and tumorigenesis.
Mnt may serve a general role as a Myc (show MYC Proteins) antagonist.[Review]
Mnt represses Myc target genes and Myc functions as an oncogene by relieving Mnt-mediated repression
Loss of protein Mnt in mice results in decreased viability, defective embryonic growth and craniofacial defects.
These results demonstrate that Mnt-Myc (show MYC Proteins) antagonism plays a fundamental role in regulating cell cycle entry and proliferation.
Mnt is expressed both in growth-arrested and proliferating mouse fibroblasts and is phosphorylated when resting cells are induced to re-enter the cell cycle
Mnt functions as a tumor suppressor and reveal a critical and surprising role for Mnt in the regulation of T-cell development and in T-cell-dependent immune homeostasis.
The switch from Mnt-Max to Myc (show MYC Proteins)-Max during bile duct ligation (cholestasis) and in hepatocytes treated with lithocholic acid is responsible for the induction in p53 (show TP53 Proteins) and cyclin D1 (show CCND1 Proteins) expression and contributes to apoptosis.
Here we review the activities of MYC (show MYC Proteins), MNT and other MAX interacting proteins in the setting of T and B cell activation (show BLNK Proteins) and oncogenesis
The data demonstrate that the balance between c-Myc and Mnt activity determines the transcriptional outcome of the hTERT promoter by modulation of the chromatin architecture.
The results suggest that MNT, via interaction with Nck1 (show NCK1 Proteins), inhibits hepatoma cell migration.
downregulation MYCN was reflected in a decreased MYCN/Max DNA-binding activity while the Mnt/Max binding did not change during differentiation
Serum stimulation of quiescent cells results in phosphorylation of Mnt and disruption of the critical Mnt-mSin3-HDAC1 (show HDAC1 Proteins) interaction. This in turn leads to increased expression of the Myc (show MYC Proteins)/Mnt target gene cyclin D2 (show CCND2 Proteins). Review.
Mad1, Mxi1 and Rox genes were expressed and displayed mutations in haematological malignancies.
Mxd1 (show MXD1 Proteins) D112a and Max N78a and H81d, which are located in the leucine zippers of the proteins, can dictate the specificity of heterodimerization and whether or not the Mxd1 (show MXD1 Proteins)/Max/DNA complex forms.
Missense mutations in Mad1, Mxi1 and Rox were found in acute leukemia patients.
The Myc/Max/Mad network comprises a group of transcription factors that co-interact to regulate gene-specific transcriptional activation or repression. This gene encodes a protein member of the Myc/Max/Mad network. This protein has a basic-Helix-Loop-Helix-zipper domain (bHLHzip) with which it binds the canonical DNA sequence CANNTG, known as the E box, following heterodimerization with Max proteins. This protein is likely a transcriptional repressor and an antagonist of Myc-dependent transcriptional activation and cell growth. This protein represses transcription by binding to DNA binding proteins at its N-terminal Sin3-interaction domain.
max-binding protein MNT
, myc antagonist MNT
, MAX binding protein
, Max-interacting protein
, class D basic helix-loop-helix protein 3
, max binding protein